PBPB_ECOLI
ID PBPB_ECOLI Reviewed; 844 AA.
AC P02919; P75664;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Penicillin-binding protein 1B;
DE Short=PBP-1b;
DE Short=PBP1b;
DE AltName: Full=Murein polymerase;
DE Includes:
DE RecName: Full=Penicillin-insensitive transglycosylase;
DE EC=2.4.1.129 {ECO:0000269|PubMed:19458048, ECO:0000269|PubMed:6389538};
DE AltName: Full=Peptidoglycan TGase;
DE AltName: Full=Peptidoglycan glycosyltransferase;
DE Includes:
DE RecName: Full=Penicillin-sensitive transpeptidase;
DE EC=3.4.16.4 {ECO:0000269|PubMed:6389538};
DE AltName: Full=DD-transpeptidase;
GN Name=mrcB; Synonyms=pbpF, ponB; OrderedLocusNames=b0149, JW0145;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3882429; DOI=10.1111/j.1432-1033.1985.tb08768.x;
RA Broome-Smith J.K., Edelman A., Yousif S., Spratt B.G.;
RT "The nucleotide sequences of the ponA and ponB genes encoding penicillin-
RT binding protein 1A and 1B of Escherichia coli K12.";
RL Eur. J. Biochem. 147:437-446(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 103
RP AND 754.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 497-525.
RC STRAIN=K12;
RX PubMed=3920658; DOI=10.1073/pnas.82.7.1999;
RA Keck W., Glauner B., Schwarz U., Broome-Smith J.K., Spratt B.G.;
RT "Sequences of the active-site peptides of three of the high-Mr penicillin-
RT binding proteins of Escherichia coli K-12.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1999-2003(1985).
RN [6]
RP CATALYTIC ACTIVITY.
RX PubMed=6389538; DOI=10.1016/s0021-9258(18)89835-0;
RA Nakagawa J., Tamaki S., Tomioka S., Matsuhashi M.;
RT "Functional biosynthesis of cell wall peptidoglycan by polymorphic
RT bifunctional polypeptides. Penicillin-binding protein 1Bs of Escherichia
RT coli with activities of transglycosylase and transpeptidase.";
RL J. Biol. Chem. 259:13937-13946(1984).
RN [7]
RP CHARACTERIZATION.
RX PubMed=8645198; DOI=10.1042/bj3160149;
RA Wang C.C., Schultz D.R., Nicholas R.A.;
RT "Localization of a putative second membrane association site in penicillin-
RT binding protein 1B of Escherichia coli.";
RL Biochem. J. 316:149-156(1996).
RN [8]
RP TOPOLOGY.
RX PubMed=9244263; DOI=10.1128/jb.179.15.4761-4767.1997;
RA Lefevre F., Remy M.-H., Masson J.-M.;
RT "Topographical and functional investigation of Escherichia coli penicillin-
RT binding protein 1b by alanine stretch scanning mutagenesis.";
RL J. Bacteriol. 179:4761-4767(1997).
RN [9]
RP TOPOLOGY.
RX PubMed=3330753; DOI=10.1111/j.1365-2958.1987.tb00533.x;
RA Edelman A., Bowler L., Broome-Smith J.K., Spratt B.G.;
RT "Use of a beta-lactamase fusion vector to investigate the organization of
RT penicillin-binding protein 1B in the cytoplasmic membrane of Escherichia
RT coli.";
RL Mol. Microbiol. 1:101-106(1987).
RN [10]
RP DIMERIZATION.
RX PubMed=1885547; DOI=10.1128/jb.173.18.5740-5746.1991;
RA Zijderveld C.A., Aarsman M.E., den Blaauwen T., Nanninga N.;
RT "Penicillin-binding protein 1B of Escherichia coli exists in dimeric
RT forms.";
RL J. Bacteriol. 173:5740-5746(1991).
RN [11]
RP INTERACTION WITH MIPA AND MLTA.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=10037771; DOI=10.1074/jbc.274.10.6726;
RA Vollmer W., von Rechenberg M., Hoeltje J.-V.;
RT "Demonstration of molecular interactions between the murein polymerase
RT PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of
RT Escherichia coli.";
RL J. Biol. Chem. 274:6726-6734(1999).
RN [12]
RP ACTIVE SITE SER-510, AND MUTAGENESIS OF GLU-233; ASP-234 AND GLU-290.
RC STRAIN=EJ801;
RX PubMed=10564478; DOI=10.1046/j.1365-2958.1999.01612.x;
RA Terrak M., Ghosh T.K., van Heijenoort J., Van Beeumen J., Lampilas M.,
RA Aszodi J., Ayala J.A., Ghuysen J.-M., Nguyen-Disteche M.;
RT "The catalytic, glycosyl transferase and acyl transferase modules of the
RT cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of
RT Escherichia coli.";
RL Mol. Microbiol. 34:350-364(1999).
RN [13]
RP REVIEW.
RX PubMed=9841666; DOI=10.1128/mmbr.62.4.1079-1093.1998;
RA Goffin C., Ghuysen J.-M.;
RT "Multimodular penicillin-binding proteins: an enigmatic family of orthologs
RT and paralogs.";
RL Microbiol. Mol. Biol. Rev. 62:1079-1093(1998).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 58-804 IN COMPLEX WITH
RP MOENOMYCIN, PARTIAL PROTEIN SEQUENCE, INTERACTION WITH MLTA; UVRA; FTSL AND
RP FTSN, MEMBRANE TOPOLOGY, CATALYTIC ACTIVITY, DOMAIN, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=19458048; DOI=10.1073/pnas.0904030106;
RA Sung M.-T., Lai Y.-T., Huang C.-Y., Chou L.-Y., Shih H.-W., Cheng W.-C.,
RA Wong C.-H., Ma C.;
RT "Crystal structure of the membrane-bound bifunctional transglycosylase
RT PBP1b from Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8824-8829(2009).
CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC from the lipid intermediates. The enzyme has a penicillin-insensitive
CC transglycosylase N-terminal domain (formation of linear glycan strands)
CC and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC linking of the peptide subunits).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000269|PubMed:19458048, ECO:0000269|PubMed:6389538};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000269|PubMed:6389538};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBUNIT: Forms a trimeric complex with MipA and MltA. Has also been
CC shown to exist as monomer or homodimer; homodimer of Alpha and Gamma
CC isozymes can be found. Interacts with UvrA, FtsL and FtsN.
CC {ECO:0000269|PubMed:10037771, ECO:0000269|PubMed:19458048}.
CC -!- INTERACTION:
CC P02919; P0AD68: ftsI; NbExp=3; IntAct=EBI-909769, EBI-548564;
CC P02919; P29131: ftsN; NbExp=7; IntAct=EBI-909769, EBI-1134233;
CC P02919; P0AB38: lpoB; NbExp=4; IntAct=EBI-909769, EBI-3405489;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Alpha; Synonyms=Long;
CC IsoId=P02919-1; Sequence=Displayed;
CC Name=Gamma; Synonyms=Short;
CC IsoId=P02919-2; Sequence=VSP_018737;
CC -!- DOMAIN: The UvrB domain 2 homolog region (UB2H domain) is important for
CC interaction with MltA. {ECO:0000269|PubMed:19458048}.
CC -!- MISCELLANEOUS: A third isozyme, Beta, lacking the first 25 N-terminal
CC amino acids of the isoform Alpha and a fourth isozyme, Delta, have been
CC found, but seem to result from the artifactual degradation of the
CC isoform Alpha and isoform Gamma respectively.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA26099.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X02163; CAA26098.1; -; Genomic_DNA.
DR EMBL; X02163; CAA26099.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73260.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96725.2; -; Genomic_DNA.
DR PIR; E64738; ZPECPB.
DR RefSeq; NP_414691.1; NC_000913.3.
DR RefSeq; WP_000918162.1; NZ_STEB01000032.1.
DR PDB; 3FWL; X-ray; 3.09 A; A=58-804.
DR PDB; 3VMA; X-ray; 2.16 A; A=58-804.
DR PDB; 5FGZ; X-ray; 2.85 A; A=58-804.
DR PDB; 5HL9; X-ray; 2.70 A; A=58-804.
DR PDB; 5HLA; X-ray; 2.36 A; A=58-804.
DR PDB; 5HLB; X-ray; 2.42 A; A=58-804.
DR PDB; 5HLD; X-ray; 2.31 A; A=58-804.
DR PDB; 6FZK; NMR; -; A=108-200.
DR PDB; 6G5R; NMR; -; A=108-200.
DR PDB; 6YN0; X-ray; 2.40 A; A=58-804.
DR PDB; 7LQ6; EM; 3.28 A; A=58-804.
DR PDBsum; 3FWL; -.
DR PDBsum; 3VMA; -.
DR PDBsum; 5FGZ; -.
DR PDBsum; 5HL9; -.
DR PDBsum; 5HLA; -.
DR PDBsum; 5HLB; -.
DR PDBsum; 5HLD; -.
DR PDBsum; 6FZK; -.
DR PDBsum; 6G5R; -.
DR PDBsum; 6YN0; -.
DR PDBsum; 7LQ6; -.
DR AlphaFoldDB; P02919; -.
DR SMR; P02919; -.
DR BioGRID; 4260880; 259.
DR DIP; DIP-10252N; -.
DR IntAct; P02919; 15.
DR STRING; 511145.b0149; -.
DR BindingDB; P02919; -.
DR ChEMBL; CHEMBL1814; -.
DR DrugBank; DB01602; Bacampicillin.
DR DrugBank; DB00578; Carbenicillin.
DR DrugBank; DB09319; Carindacillin.
DR DrugBank; DB01414; Cefacetrile.
DR DrugBank; DB01327; Cefazolin.
DR DrugBank; DB00274; Cefmetazole.
DR DrugBank; DB01328; Cefonicid.
DR DrugBank; DB01329; Cefoperazone.
DR DrugBank; DB01331; Cefoxitin.
DR DrugBank; DB00430; Cefpiramide.
DR DrugBank; DB11367; Cefroxadine.
DR DrugBank; DB00438; Ceftazidime.
DR DrugBank; DB01415; Ceftibuten.
DR DrugBank; DB01332; Ceftizoxime.
DR DrugBank; DB09050; Ceftolozane.
DR DrugBank; DB00689; Cephaloglycin.
DR DrugBank; DB01000; Cyclacillin.
DR DrugBank; DB06211; Doripenem.
DR DrugBank; DB00303; Ertapenem.
DR DrugBank; DB01598; Imipenem.
DR DrugBank; DB04570; Latamoxef.
DR DrugCentral; P02919; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR jPOST; P02919; -.
DR PaxDb; P02919; -.
DR PRIDE; P02919; -.
DR EnsemblBacteria; AAC73260; AAC73260; b0149.
DR EnsemblBacteria; BAB96725; BAB96725; BAB96725.
DR GeneID; 944843; -.
DR KEGG; ecj:JW0145; -.
DR KEGG; eco:b0149; -.
DR PATRIC; fig|1411691.4.peg.2132; -.
DR EchoBASE; EB0600; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_7_6; -.
DR InParanoid; P02919; -.
DR OMA; VHGMGLA; -.
DR PhylomeDB; P02919; -.
DR BioCyc; EcoCyc:EG10605-MON; -.
DR BioCyc; MetaCyc:EG10605-MON; -.
DR BRENDA; 2.4.1.129; 2026.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P02919; -.
DR PRO; PR:P02919; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
DR GO; GO:0008658; F:penicillin binding; IDA:EcoCyc.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IDA:EcoCyc.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IDA:EcoCyc.
DR GO; GO:0071433; P:cell wall repair; IDA:EcoCyc.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:EcoCyc.
DR GO; GO:0051518; P:positive regulation of bipolar cell growth; IDA:EcoliWiki.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR GO; GO:0010165; P:response to X-ray; IMP:EcoCyc.
DR Gene3D; 1.10.3810.10; -; 1.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR032730; PBP1b_TM.
DR InterPro; IPR011813; PBP_1b.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR028166; UB2H.
DR Pfam; PF14812; PBP1_TM; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR Pfam; PF14814; UB2H; 1.
DR PIRSF; PIRSF002799; PBP_1b; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR TIGRFAMs; TIGR02071; PBP_1b; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Antibiotic resistance;
KW Carboxypeptidase; Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Direct protein sequencing;
KW Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
KW Peptidoglycan synthesis; Protease; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..844
FT /note="Penicillin-binding protein 1B"
FT /id="PRO_0000012145"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..87
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT TOPO_DOM 88..844
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..250
FT /note="Membrane association"
FT REGION 109..200
FT /note="UvrB domain 2 homolog"
FT REGION 195..367
FT /note="Transglycosylase"
FT REGION 444..736
FT /note="Transpeptidase"
FT REGION 793..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 233
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000305|PubMed:10564478"
FT ACT_SITE 510
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000269|PubMed:10564478"
FT VAR_SEQ 1..45
FT /note="Missing (in isoform Gamma)"
FT /evidence="ECO:0000305"
FT /id="VSP_018737"
FT MUTAGEN 233
FT /note="E->Q: Loss of wild-type glycan chain elongation
FT activity. No complementation in strain defective in PBP-
FT 1b."
FT /evidence="ECO:0000269|PubMed:10564478"
FT MUTAGEN 234
FT /note="D->N: 7-fold decrease in catalytic activity. No
FT complementation in strain defective in PBP-1b."
FT /evidence="ECO:0000269|PubMed:10564478"
FT MUTAGEN 290
FT /note="E->Q: 11-fold decrease in catalytic activity. Shows
FT complementation activity in strain defective in PBP-1b."
FT /evidence="ECO:0000269|PubMed:10564478"
FT CONFLICT 103
FT /note="P -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="P -> PTP (in Ref. 2)"
FT /evidence="ECO:0000305"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:3FWL"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5HL9"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6FZK"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:3VMA"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:5HLD"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:3FWL"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:3FWL"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 268..276
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:5FGZ"
FT HELIX 284..300
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:3VMA"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 327..335
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 344..355
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:3VMA"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 366..382
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:5HLB"
FT HELIX 388..395
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 412..426
FT /evidence="ECO:0007829|PDB:3VMA"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:5HLD"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 444..464
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 471..478
FT /evidence="ECO:0007829|PDB:3VMA"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 483..488
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:5HL9"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:5HLD"
FT HELIX 500..503
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 509..512
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 513..521
FT /evidence="ECO:0007829|PDB:3VMA"
FT TURN 524..526
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:5HL9"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:5HL9"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 565..570
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 574..584
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 586..596
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 607..611
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 618..629
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 640..644
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:3FWL"
FT STRAND 650..653
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 664..679
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 684..689
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 691..693
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 696..701
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 703..705
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 706..713
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 715..724
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 737..749
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 763..768
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 774..777
FT /evidence="ECO:0007829|PDB:3VMA"
FT STRAND 780..786
FT /evidence="ECO:0007829|PDB:3VMA"
FT HELIX 792..797
FT /evidence="ECO:0007829|PDB:3VMA"
SQ SEQUENCE 844 AA; 94293 MW; CED0A19FAC73961E CRC64;
MAGNDREPIG RKGKPTRPVK QKVSRRRYED DDDYDDYDDY EDEEPMPRKG KGKGKGRKPR
GKRGWLWLLL KLAIVFAVLI AIYGVYLDQK IRSRIDGKVW QLPAAVYGRM VNLEPDMTIS
KNEMVKLLEA TQYRQVSKMT RPGEFTVQAN SIEMIRRPFD FPDSKEGQVR ARLTFDGDHL
ATIVNMENNR QFGFFRLDPR LITMISSPNG EQRLFVPRSG FPDLLVDTLL ATEDRHFYEH
DGISLYSIGR AVLANLTAGR TVQGASTLTQ QLVKNLFLSS ERSYWRKANE AYMALIMDAR
YSKDRILELY MNEVYLGQSG DNEIRGFPLA SLYYFGRPVE ELSLDQQALL VGMVKGASIY
NPWRNPKLAL ERRNLVLRLL QQQQIIDQEL YDMLSARPLG VQPRGGVISP QPAFMQLVRQ
ELQAKLGDKV KDLSGVKIFT TFDSVAQDAA EKAAVEGIPA LKKQRKLSDL ETAIVVVDRF
SGEVRAMVGG SEPQFAGYNR AMQARRSIGS LAKPATYLTA LSQPKIYRLN TWIADAPIAL
RQPNGQVWSP QNDDRRYSES GRVMLVDALT RSMNVPTVNL GMALGLPAVT ETWIKLGVPK
DQLHPVPAML LGALNLTPIE VAQAFQTIAS GGNRAPLSAL RSVIAEDGKV LYQSFPQAER
AVPAQAAYLT LWTMQQVVQR GTGRQLGAKY PNLHLAGKTG TTNNNVDTWF AGIDGSTVTI
TWVGRDNNQP TKLYGASGAM SIYQRYLANQ TPTPLNLVPP EDIADMGVDY DGNFVCSGGM
RILPVWTSDP QSLCQQSEMQ QQPSGNPFDQ SSQPQQQPQQ QPAQQEQKDS DGVAGWIKDM
FGSN
